› 3zpd

Solution NMR

Solution structure of the FimH adhesin carbohydrate-binding domain

Released:
DOI: 10.2210/pdb3zpd/pdb
PDB 3zpd coloured by chain and viewed from the front.
PDB 3zpd coloured by chain and viewed from the side.
PDB 3zpd coloured by chain and viewed from the top.
Source organism: Escherichia coli J96
Primary publication:
Study of the structural and dynamic effects in the FimH adhesin upon α-D-heptyl mannose binding.
Vanwetswinkel S, Volkov AN, Sterckx YG, Garcia-Pino A, Buts L, Vranken WF, Bouckaert J, Roy R, Wyns L, Van Nuland NA
J. Med. Chem. (2014)
PMID: 24476493

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FimH_man-bind domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 16.92 KDa
Source organism: Escherichia coli J96
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A2IC68 (Residues: 10-167; Coverage: 70%)
Gene name: fimH
Sequence domains: FimH, mannose binding
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 94%
Refinement method: RECOORD
Chemical shifts: BMR19066  
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

FimH and Anti-Adhesive Therapeutics: A Disarming Strategy Against Uropathogens.
Sarshar et al. (2020)
4 more

1 mention without citation

Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system.
Rabbani et al. (2018)